関: carboxyesterase、carboxylic ester hydrolase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/02/19 00:09:28」(JST)

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In enzymology, a carboxylesterase (EC 3.1.1.1) is an enzyme that catalyzes the chemical reaction

a carboxylic ester + H₂O an alcohol + a carboxylate

Thus, the two substrates of this enzyme are carboxylic ester and H₂O, whereas its two products are alcohol and carboxylate.

Most enzymes from this group belong to the superfamily of hydrolases with alpha/beta protein fold (so called Alpha/beta hydrolase fold), specifically those acting on carboxylic ester bonds. Some exceptions include an esterase with beta-lactamase like structure (PDB 1ci8). The carboxylesterase family of evolutionarily related proteins (those with clear sequence homology to each other) includes a number of proteins with different substrate specificities, such as acetylcholinesterases.

Nomenclature

Carboxylesterase is an enzyme that is capable of hydrolyzing a wide variety of carboxylic acid esters. Although its metabolic function is unclear, the enzyme is widely distributed in nature, being especially common in mammalian liver. Carboxylesterase belongs to the class of serine hydrolases which includes Chymotrypsin and Acetylcholinesterase.

The systematic name of this enzyme class is carboxylic-ester hydrolase. Examples of carboxyesterases include:

ali-esterase,
alpha-carboxylesterase,
B-esterase,
butyrate esterase,
butyryl esterase,
carboxyesterase,
carboxyl ester hydrolase,
carboxylate esterase,
carboxylic acid esterase,
carboxylic esterase,
esterase A,
esterase B,
esterase D,
methylbutyrase,
methylbutyrase,
methylbutyrate esterase,
monobutyrase,
nonspecific carboxylesterase,
procaine esterase,
propionyl esterase,
serine esterase,
triacetin esterase,
vitamin A esterase, and
cocaine esterase.

The last enzyme also participates in alkaloid biosynthesis.

Genes

Humans genes that encode carboxylesterase enzymes include:

CES1
CES2
CES3
CES4
CES7
CES8

Structural studies

As of late 2007, 38 structures have been solved for this class of enzymes, with PDB accession codes 1AUO, 1AUR, 1CI8, 1CI9, 1EVQ, 1JJI, 1K4Y, 1L7Q, 1L7R, 1MX1, 1MX5, 1MX9, 1QZ3, 1R1D, 1TQH, 1U4N, 1YA4, 1YA8, 1YAH, 1YAJ, 2C7B, 2DQY, 2DQZ, 2DR0, 2FJ0, 2H1I, 2H7C, 2HM7, 2HRQ, 2HRR, 2JEY, 2JEZ, 2JF0, 2O7R, 2O7V, 2OGS, 2OGT, and 2R11.

References

Augusteyn RC, de Jersey J, Webb EC, Zerner B (1969). "On the homology of the active-site peptides of liver carboxylesterases". Biochim. Biophys. Acta. 171 (1): 128–37. PMID 4884138.
Barker DL, Jencks WP (1969). "Pig liver esterase. Physical properties". Biochemistry. 8 (10): 3879–89. doi:10.1021/bi00838a001. PMID 4981346.
Bertram J, Krisch K (1969). "Hydrolysis of vitamin A acetate by unspecific carboxylesterases from liver and kidney". Eur. J. Biochem. 11 (1): 122–6. doi:10.1111/j.1432-1033.1969.tb00748.x. PMID 5353595.
BURCH J (1954). "The purification and properties of horse liver esterase". Biochem. J. 58 (3): 415–26. PMC 1269916. PMID 13208632. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1269916/.
Horgan DJ, Stoops JK, Webb EC, Zerner B (1969). "Carboxylesterases (EC 3.1.1). A large-scale purification of pig liver carboxylesterase". Biochemistry. 8 (5): 2000–6. doi:10.1021/bi00833a033. PMID 5785220.
Malhotra OP and Philip G (1966). "Specificity of goat intestinal esterase". Biochem. Z. 346: 386–402.
Mentlein R, Schumann M, Heymann E (1984). "Comparative chemical and immunological characterization of five lipolytic enzymes (carboxylesterases) from rat liver microsomes". Arch. Biochem. Biophys. 234 (2): 612–21. doi:10.1016/0003-9861(84)90311-4. PMID 6208846.
Runnegar MT, Scott K, Webb EC, Zerner B (1969). "Carboxylesterases (EC 3.1.1). Purification and titration of ox liver carboxylesterase". Biochemistry. 8 (5): 2013–8. doi:10.1021/bi00833a035. PMID 5785222.

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English Journal

Fluoxetine reduces CES1, CES2, and CYP3A4 expression through decreasing PXR and increasing DEC1 in HepG2 cells.

Shang W1, Liu J1, Chen R1, Ning R1, Xiong J1, Liu W1, Mao Z2, Hu G1, Yang J1.
Xenobiotica; the fate of foreign compounds in biological systems.Xenobiotica.2016 May;46(5):393-405. doi: 10.3109/00498254.2015.1082209. Epub 2015 Sep 4.
1. This study investigated the mechanisms of the decreases of carboxylesterases (CES) and cytochrome P4503A4 (CYP3A4) and the enzymatic activities induced by fluoxetine (FLX) in HepG2 cells. We found that FLX decreased the carboxylesterase 1 (CES1) and carboxylesterase 2 (CES2) expression and the
PMID 26340669

Design, synthesis, and structure-activity relationship study of glycyrrhetinic acid derivatives as potent and selective inhibitors against human carboxylesterase 2.

Zou LW1, Li YG1, Wang P1, Zhou K2, Hou J3, Jin Q1, Hao DC4, Ge GB5, Yang L6.
European journal of medicinal chemistry.Eur J Med Chem.2016 Apr 13;112:280-8. doi: 10.1016/j.ejmech.2016.02.020. Epub 2016 Feb 9.
Human carboxylesterase 2 (hCE2), one of the major carboxylesterases in the human intestine and various tumour tissues, plays important roles in the oral bioavailability and treatment outcomes of ester- or amide-containing drugs or prodrugs, such as anticancer agents CPT-11 (irinotecan) and LY2334737
PMID 26900660

Identification of biotransformation enzymes in the antennae of codling moth Cydia pomonella.

Huang X1, Liu L1, Su X2, Feng J3.
Gene.Gene.2016 Apr 10;580(1):73-9. doi: 10.1016/j.gene.2016.01.008. Epub 2016 Jan 8.
Biotransformation enzymes are found in insect antennae and play a critical role in degrading xenobiotics and odorants. In Cydia pomonella, we identified 26 biotransformation enzymes. Among these enzymes, twelve carboxylesterases (CXEs), two aldehyde oxidases (AOXs) and six alcohol dehydrogenases (AD
PMID 26778204

Japanese Journal

カルボキシルエステラーゼ研究の現状とプロドラッグ体内動態の予測

今井輝子
薬剤学 = The archives of practical pharmacy 71(4), 198-206, 2011-07-01
NAID 10029101099

Identification of the Catalytic Residues of Carboxylesterase from Arthrobacter globiformis by Diisopropyl Fluorophosphate-Labeling and Site-Directed Mutagenesis

NISHIZAWA Masako,YABUSAKI Yoshiyasu,KANAOKA Masaharu
Bioscience, biotechnology, and biochemistry 75(1), 89-94, 2011-01-23
… The role of amino acid residues in the enzymatic activity of carboxylesterase from Arthrobacter globiformis was analyzed by diisopropyl fluorophosphate (DFP) labeling and site-directed mutagenesis. …
NAID 10027896792

Characterization of a Carboxylesterase from Burkhokderia ferrariae L-2 which Enhances the Flavor of Cheese

Mase Tamio,Hisamatsu Noriko,Murata Yuu [他]
椙山女学園大学研究論集自然科学篇 (42), 101-107, 2011
NAID 40018723381

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リンク元	「carboxylic ester hydrolase」「カルボキシエステラーゼ」「carboxyesterase」

「carboxylic ester hydrolase」

carboxylesterase
Identifiers
EC number	3.1.1.1
CAS number	9016-18-6
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins